Insight into the co-solvent induced conformational changes and aggregation of bovine β-lactoglobulin

Pal, Sampa; Maity, Sanhita; Sardar, Subrata; Chakraborty, Jishnu; Halder, Umesh Chandra

doi:10.1016/j.ijbiomac.2015.11.055

Cited by 16 publications

(8 citation statements)

References 72 publications

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“…Fibrils formed during heating in water at 90 °C and pH 2.0 disassemble and then reassemble into a different type of fibril when incubated in aqueous ethanol (Jordens, Adamcik, Amar‐Yuli, & Mezzenga, ). The presence of acetonitrile and benzyl alcohol at neutral pH can also induce amyloid‐like structures (Pal, Maity, Sardar, Chakraborty, & Halder, ).…”

Section: Bovine Milk Proteinsmentioning

confidence: 99%

Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins

Lambrecht

Jansens

Rombouts

et al. 2019

Comp Rev Food Sci Food Safe

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Both intrinsic and extrinsic factors impact amyloid formation of food proteins. We here review the impact of various conditions and food constituents on amyloid fibrillation of milk and legume proteins. Much less is known about casein and legume protein amyloid‐like fibril formation than about that of whey proteins such as β‐lactoglobulin, α‐lactalbumin, and bovine serum albumin. Proteins of both sources are often studied after heating under strong acidic (pH < 3) conditions. The latter induces changes in protein conformation and often peptide hydrolysis. At higher pH values, alcohols, chaotropic and/or reducing agents induce the conformational changes required to enhance fibrillation. Different types of food proteins can impact each other's fibrillation. Also, the presence of other food constituents can enhance or reduce it. No general conclusions on the mechanisms or impact of different food constituents on food proteins can be made. Optimal conditions for AF formation, that is, heating for several days at low pH, are rare in food processing. However, this does not exclude the possibility of AF formation in food products. For example, slow cooking of hydrolyzed proteins may enhance it. Future research should focus on the prevalence of AFs in complex food systems or model systems relevant for food processing.

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Section: Bovine Milk Proteinsmentioning

confidence: 99%

Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins

Lambrecht

Jansens

Rombouts

et al. 2019

Comp Rev Food Sci Food Safe

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“…Congo red (CR) spectrophotometric method has been commonly used to analyze the solution conformation of ionic biopolymer. The procedure of CR-polysaccharide binding experiment was performed according to the method of Pal et al with some modifications (Pal et al, 2016). CR solution (concentration of 91 μmol/L) and SeASP solutions (concentrations of 0.2~2 mg/mL) were prepared in distilled water at room temperature.…”

Section: Congo Red Binding Studiesmentioning

confidence: 99%

Synthesis of selenium-containing Artemisia sphaerocephala polysaccharides: Solution conformation and anti-tumor activities in vitro

Wang

Bao

et al. 2016

Carbohydrate Polymers

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It has been reported in our previous work that selenized Artemisia sphaerocephala polysaccharides (SeASPs) with the Se content range of 168-1703μg/g were synthesized by using Na2SeO3/HNO3/BaCl2 system. In the present work, the solution property of SeASP was studied by using size exclusion chromatography combined with multi angle laser light scattering (SEC-MALLS). A decrease in df values indicated that SeASPs with different conformational features that were highly dependent on MW. SeASPs exhibited a more rigid conformation (df value of 1.29-1.52) in low molecular weight range (MW of 1.026-1.426×10(4)g/mol) and compact spherical conformation in high molecular weight range (MW of 2.268-4.363×10(4)g/mol). It could be due to the degradation of polysaccharide chains in HNO3, which was supported in monosaccharide composition analysis. Congo red (CR) spectrophotometric method and atomic force microscopy (AFM) results also confirmed the conformational transition and the evidence on the shape of the rigid chains. In vitro anti-tumor assays, SeASP2 displayed greater anti-proliferative effects against three tumor cell lines (hepatocellular carcinoma HepG-2 cells, lung adenocarcinom A549 cells and cervical squamous carcinoma Hela cells) in a dose-dependent manner. This suggested that selenylation could significantly enhance the anti-tumor activities of polysaccharide derivatives in vitro.

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“…Whey protein at 5% showed a significant shift from 490 to 515 nm, showing the formation of maximum amyloid fibrils at this concentration. These changes in absorbance are due to CR gets trapped into the cluster of β-sheet peptide backbone of the aggregates of β-lactoglobulin and α-lactalbumin [70]. These results indicated that a significant change in the absorbance spectra was observed at concentrations higher than 3%, which demonstrated that whey solutions from this concentration after heat treatment aggregated into amyloid fibrils.…”

Section: Red Congomentioning

confidence: 87%

Section: Red Congomentioning

confidence: 99%

Preparation of a Hybrid Membrane from Whey Protein Fibrils and Activated Carbon to Remove Mercury and Chromium from Water

et al. 2020

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Water contamination by mercury and chromium has a direct effect in human health. A promising technology to remove heavy metals by membrane filtration is the use of hybrid membranes produced with whey protein fibrils (WPF) and activated carbon (AC). In this study, the best conditions to produce WPF by heat treatment were determined to maximize the removal of mercury and chromium from water using a central composed design. The results indicated that the best conditions to prepare WPF were 74 °C, 7 h and 3.8% of whey protein with adsorption capacities of 25 and 18 mg/g and removal efficiencies of 81 and 57% for mercury and chromium, respectively. WPF and AC were used to prepare a hybrid membrane that was characterized using transmission electron microscopy, atomic force microscopy, scanning electron microscopy, Fourier transform infrared spectroscopy and Brunauer–Emmett–Teller surface area measurements. Batch filtration experiments were performed with the hybrid membrane for chromium and mercury removal at 25, 50 and 100 mg/L to determine its adsorption capacities. A high performance of the hybrid membrane was demonstrated removing efficiently mercury and chromium from water, thus supporting more than ten filtration cycles.

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Insight into the co-solvent induced conformational changes and aggregation of bovine β-lactoglobulin

Cited by 16 publications

References 72 publications

Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins

Conditions Governing Food Protein Amyloid Fibril Formation. Part II: Milk and Legume Proteins

Synthesis of selenium-containing Artemisia sphaerocephala polysaccharides: Solution conformation and anti-tumor activities in vitro

Preparation of a Hybrid Membrane from Whey Protein Fibrils and Activated Carbon to Remove Mercury and Chromium from Water

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